| Title: |
Proteasome-associated ubiquitin ligase relays target plant hormone-specific transcriptional activators |
| Authors: |
Wang, Zhishuo; Orosa-Puente, Beatriz; Nomoto, Mika; Grey, Heather; Potuschak, Thomas; Matsuura, Takakazu; Mori, Izumi; Tada, Yasuomi; Genschik, Pascal; Spoel, Steven |
| Contributors: |
School of Biological Sciences Edinburgh; The University of Edinburgh; Center for Gene Research Nagoya, Japan; Nagoya University; Institut de Biologie Moléculaire des Plantes (IBMP); Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS); This work was supported by the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation program, grant agreement no. 678511 (to S.H.S.), Biotechnology and Biological Sciences Research Council (BBSRC) grant BB/S016767/1 (to S.H.S.), Darwin Trust PhD studentship (to Z.W.), Royal Society International Exchanges grant IEC\R3\170118 (to S.H.S. and Y.T.), SPS Grant-in-Aid for Scientific Research (B) grant 16H05065 (to Y.T.), and Agence Nationale de la Recherche (ANR) grant ANR-10-IDEX-0002 and IMCBio ANR-17-EURE-0023 (to T.P. and P.G.).; ANR-17-EURE-0023,IMCBio,Integrative Molecular and Cellular Biology(2017); ANR-10-IDEX-0002,UNISTRA,Par-delà les frontières, l'Université de Strasbourg(2010); European Project: 678511,ERC-2015-STG,ERC-2015-STG,IMMUNE-EXPRESS(2016) |
| Source: |
ISSN: 2375-2548 ; Science Advances ; https://cnrs.hal.science/hal-03843751 ; Science Advances , 2022, 8 (42), ⟨10.1126/sciadv.abn4466⟩. |
| Publisher Information: |
CCSD; American Association for the Advancement of Science (AAAS) |
| Publication Year: |
2022 |
| Subject Terms: |
[SDV]Life Sciences [q-bio] |
| Description: |
International audience ; The ubiquitin-proteasome system is vital to hormone-mediated developmental and stress responses in plants. Ubiquitin ligases target hormone-specific transcriptional activators (TAs) for degradation, but how TAs are processed by proteasomes remains unknown. We report that in Arabidopsis , the salicylic acid– and ethylene-responsive TAs, NPR1 and EIN3, are relayed from pathway-specific ubiquitin ligases to proteasome-associated HECT-type UPL3/4 ligases. Activity and stability of NPR1 were regulated by sequential action of three ubiquitin ligases, including UPL3/4, while proteasome processing of EIN3 required physical handover between ethylene-responsive SCF EBF2 and UPL3/4 ligases. Consequently, UPL3/4 controlled extensive hormone-induced developmental and stress-responsive transcriptional programs. Thus, our findings identify unknown ubiquitin ligase relays that terminate with proteasome-associated HECT-type ligases, which may be a universal mechanism for processive degradation of proteasome-targeted TAs and other substrates. |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| Relation: |
info:eu-repo/grantAgreement//678511/EU/Proteasome-Mediated Gene Expression in Plant Immunity/IMMUNE-EXPRESS; PUBMEDCENTRAL: PMC9586472 |
| DOI: |
10.1126/sciadv.abn4466 |
| Availability: |
https://cnrs.hal.science/hal-03843751; https://cnrs.hal.science/hal-03843751v1/document; https://cnrs.hal.science/hal-03843751v1/file/sciadv.abn4466.pdf; https://doi.org/10.1126/sciadv.abn4466 |
| Rights: |
info:eu-repo/semantics/OpenAccess |
| Accession Number: |
edsbas.2555463A |
| Database: |
BASE |